› 3umh

X-ray diffraction
2Å resolution

X-ray structure of the E2 domain of the human amyloid precursor protein (APP) in complex with cadmium

Released:
DOI: 10.2210/pdb3umh/pdb
PDB entry 3umh coloured by chain, front view.
PDB entry 3umh coloured by chain, side view.
PDB entry 3umh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Metal binding dictates conformation and function of the amyloid precursor protein (APP) E2 domain.
Dahms SO, Könnig I, Roeser D, Gührs KH, Mayer MC, Kaden D, Multhaup G, Than ME
J Mol Biol 416 438-52 (2012)
PMID: 22245578

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138353 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Soluble APP-beta Chain: A
Molecule details ›
Chain: A
Length: 211 amino acids
Theoretical weight: 25.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05067 (Residues: 370-575; Coverage: 27%)
Gene names: A4, AD1, APP
Sequence domains: E2 domain of amyloid precursor protein
Structure domains: Amyloid precursor protein, E2 domain

Ligands and Environments

2 bound ligands:
Ligand ACT 2 x ACT
Ligand CD 9 x CD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P43
Unit cell:
a: 39.692Å b: 39.692Å c: 126.215Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.198 0.24
Expression system: Escherichia coli

Quick links

Citations

28 review citations

Oxidative stress and the amyloid beta peptide in Alzheimer's disease.
Cheignon et al. (2018)
27 more

8 mentions without citation

Mechanisms and regulation of iron trafficking across the capillary endothelial cells of the blood-brain barrier.
McCarthy et al. (2015)
7 more